CHEMICAL SYNTHESIS OF A HEAT-STABLE ENTEROTOXIN PRODUCED BY ENTEROTOXIGENIC ESCHERICHIA COLI STRAIN 18D.

Article abstract of DOI:10.1246/bcsj.57.125

Two peptides with the two primary structures of 18 amino acid residues proposed for a heat-stable enterotoxin from enterotoxigenic Escherichia coli strain 18D were synthesized by solution methods and their physicochemical and biological properties were compared with those of native toxin. One of these peptides Asn-Thr-Phe-Tyr-Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Ala-Gly-Cys- Tyr) showed the same heat-stability and **1H-NMR spectrum as those of the native toxin and evoked fluid secretion in suckling mice at a dose of 1. 5-2. 0 ng, which is similar to the effective dose of native toxin. Moreover, its toxicity was neutralized by antisera against the native toxin.